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UniProtKB/Swiss-Prot entry O43395


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRPF3_HUMAN
Primary accession number O43395
Secondary accession numbers O43446 Q5VT54
Integrated into Swiss-Prot on September 26, 2003
Sequence was last modified on September 26, 2003 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 84)
Name and origin of the protein
Protein name U4/U6 small nuclear ribonucleoprotein Prp3
Synonyms Pre-mRNA-splicing factor 3
hPrp3
U4/U6 snRNP 90 kDa protein
Gene name
Name: PRPF3
Synonyms: HPRP3, PRP3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH PRPF4 AND U4/U5/U6 SNRNPS.
DOI=10.1093/hmg/6.12.2117; PubMed=9328476 [NCBI, ExPASy, EBI, Israel, Japan]
Wang A., Forman-Kay J., Luo Y., Luo M., Chow Y.-H., Plumb J., Friesen J.D., Tsui L.-C., Heng H.H.Q., Woolford J.L. Jr., Hu J.;
"Identification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosome.";
Hum. Mol. Genet. 6:2117-2126(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 93-101; 253-267; 351-361; 409-428 AND 560-576, AND INTERACTION WITH PPIH; PRPF4 AND U4/U6 SNRNPS.
TISSUE=Neuroepithelium;
PubMed=9404889 [NCBI, ExPASy, EBI, Israel, Japan]
Horowitz D.S., Kobayashi R., Krainer A.R.;
"A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs.";
RNA 3:1374-1387(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; THR-167 AND SER-619, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[13]
STRUCTURE BY NMR OF 1-79.
RIKEN structural genomics initiative (RSGI);
"Solution structure of PWI domain in U4/U6 small nuclear ribonucleoprotein PRP3(HPRP3).";
Submitted (NOV-2005) to the PDB data bank.
[14]
VARIANTS RP18 SER-493 AND MET-494, AND TISSUE SPECIFICITY.
DOI=10.1093/hmg/11.1.87; PubMed=11773002 [NCBI, ExPASy, EBI, Israel, Japan]
Chakarova C.F., Hims M.M., Bolz H., Abu-Safieh L., Patel R.J., Papaioannou M.G., Inglehearn C.F., Keen T.J., Willis C., Moore A.T., Rosenberg T., Webster A.R., Bird A.C., Gal A., Hunt D., Vithana E.N., Bhattacharya S.S.;
"Mutations in HPRP3, a third member of pre-mRNA splicing factor genes, implicated in autosomal dominant retinitis pigmentosa.";
Hum. Mol. Genet. 11:87-92(2002).
[15]
VARIANT RP18 MET-494.
DOI=10.1167/iovs.02-0871; PubMed=12714658 [NCBI, ExPASy, EBI, Israel, Japan]
Martinez-Gimeno M., Gamundi M.J., Hernan I., Maseras M., Milla E., Ayuso C., Garcia-Sandoval B., Beneyto M., Vilela C., Baiget M., Antinolo G., Carballo M.;
"Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31 in Spanish families with autosomal dominant retinitis pigmentosa.";
Invest. Ophthalmol. Vis. Sci. 44:2171-2177(2003).
[16]
CHARACTERIZATION OF VARIANT RP18 MET-494.
DOI=10.1093/hmg/ddm300; PubMed=17932117 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez-Santos J.M., Cao H., Duan R.C., Hu J.;
"Mutation in the splicing factor Hprp3p linked to retinitis pigmentosa impairs interactions within the U4/U6 snRNP complex.";
Hum. Mol. Genet. 17:225-239(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF001947; AAC09069.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016370; AAC51926.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL611942; CAH70312.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471121; EAW53556.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000184; AAH00184.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001954; AAH01954.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00005861; -.
IPI00377152; -.
PIR T50839; T50839.
T50840; T50840.
RefSeq NP_004689.1; -.
UniGene Hs.11776
3D structure databases
PDB
1X4Q; NMR; -; A=1-79.[ExPASy / RCSB / EBI]
PDBsum 1X4Q; -.
ModBase O43395.
Protein-protein interaction databases
IntAct O43395; 7.
PTM databases
PhosphoSite O43395; -.
Organism-specific databases
GeneCards GC01P148560; -.
H-InvDB HIX0001019; -.
HGNC HGNC:17348; PRPF3.
GenAtlas PRPF3.
MIM 601414; phenotype. [NCBI / EBI]
607301; gene. [NCBI / EBI]
Orphanet 791; Retinitis pigmentosa.
PharmGKB PA134892509; -.
Gene expression databases
ArrayExpress O43395; -.
Bgee O43395; -.
CleanEx HS_PRPF3; -.
GermOnline ENSG00000117360; Homo sapiens.
Ontologies
GO
GO:0016607; Cellular component: nuclear speck (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005681; Cellular component: spliceosome (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031202; Molecular function: RNA splicing factor activity, transesterification mechanism (traceable author statement from UniProtKB).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (non-traceable author statement from UniProtKB).
GO:0050896; Biological process: response to stimulus (inferred from electronic annotation from UniProtKB-KW).
GO:0007601; Biological process: visual perception (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013881; Pre-mRNA_splic_Prp3.
IPR002483; PWI.
Graphical view of domain structure.
Pfam PF08572; PRP3; 1.
PF01480; PWI; 1.
Pfam graphical view of domain structure.
SMART SM00311; PWI; 1.
SMART graphical view of domain structure.
PROSITE PS51025; PWI; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O43395; -.
Genome annotation databases
Ensembl ENSG00000117360; Homo sapiens. [Contig view]
GeneID 9129; -.
KEGG hsa:9129; -.
Phylogenomic databases
HOGENOM O43395; -.
HOVERGEN O43395; -.
OMA O43395; NIRAKKR.
Other
NextBio 34221; -.
PMAP-CutDB O43395; -.
SOURCE PRPF3; Homo sapiens.
ProtoNet O43395.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Direct protein sequencing; Disease mutation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Retinitis pigmentosa; Sensory transduction; Spliceosome; Vision.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   683  683     U4/U6 small nuclear ribonucleoprotein Prp3. PRO_0000097044
DOMAIN   1    87  87     PWI. 
COMPBIAS   579   584  6     Poly-Val. 
MOD_RES   133   133        Phosphoserine. 
MOD_RES   164   164        Phosphoserine. 
MOD_RES   167   167        Phosphothreonine. 
MOD_RES   356   356        Phosphoserine. 
MOD_RES   619   619        Phosphoserine. 
VAR_SEQ   587   587        Missing (in isoform 2). VSP_008326
VARIANT   12    12  1     K -> N (in dbSNP:rs12736964 [NCBI]). VAR_051286 
VARIANT   493   493  1     P -> S (in RP18). VAR_046735 
VARIANT   494   494  1     T -> M (in RP18; reduces phosphorylation; impairs binding to PRPF4; impairs self-association; affects interaction with the U4/U5/U6 tri-snRNP complex; does not affect global pre-mRNA splicing). VAR_016877 
CONFLICT   142   142        I -> T (in Ref. 1; AAC09069). 
CONFLICT   273   274        EL -> SV (in Ref. 1; AAC09069). 
HELIX   5    23  19      
HELIX   28    39  12      
HELIX   44    51  8      
TURN   52    55  4      
HELIX   56    58  3      
HELIX   60    73  14      
Sequence information
Length: 683 AA [This is the length of the unprocessed precursor] Molecular weight: 77529 Da [This is the MW of the unprocessed precursor] CRC64: 4AA6AA4C99110284 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALSKRELDE LKPWIEKTVK RVLGFSEPTV VTAALNCVGK GMDKKKAADH LKPFLDDSTL 

        70         80         90        100        110        120 
RFVDKLFEAV EEGRSSRHSK SSSDRSRKRE LKEVFGDDSE ISKESSGVKK RRIPRFEEVE 

       130        140        150        160        170        180 
EEPEVIPGPP SESPGMLTKL QIKQMMEAAT RQIEERKKQL SFISPPTPQP KTPSSSQPER 

       190        200        210        220        230        240 
LPIGNTIQPS QAATFMNDAI EKARKAAELQ ARIQAQLALK PGLIGNANMV GLANLHAMGI 

       250        260        270        280        290        300 
APPKVELKDQ TKPTPLILDE QGRTVDATGK EIELTHRMPT LKANIRAVKR EQFKQQLKEK 

       310        320        330        340        350        360 
PSEDMESNTF FDPRVSIAPS QRQRRTFKFH DKGKFEKIAQ RLRTKAQLEK LQAEISQAAR 

       370        380        390        400        410        420 
KTGIHTSTRL ALIAPKKELK EGDIPEIEWW DSYIIPNGFD LTEENPKRED YFGITNLVEH 

       430        440        450        460        470        480 
PAQLNPPVDN DTPVTLGVYL TKKEQKKLRR QTRREAQKEL QEKVRLGLMP PPEPKVRISN 

       490        500        510        520        530        540 
LMRVLGTEAV QDPTKVEAHV RAQMAKRQKA HEEANAARKL TAEQRKVKKI KKLKEDISQG 

       550        560        570        580        590        600 
VHISVYRVRN LSNPAKKFKI EANAGQLYLT GVVVLHKDVN VVVVEGGPKA QKKFKRLMLH 

       610        620        630        640        650        660 
RIKWDEQTSN TKGDDDEESD EEAVKKTNKC VLVWEGTAKD RSFGEMKFKQ CPTENMAREH 

       670        680 
FKKHGAEHYW DLALSESVLE STD 

O43395 in FASTA format

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